INTERACTIONS OF APOLIPOPROTEIN A-I N- AND C-TERMINI

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们实验室以前的工作和文献数据一直表明，人类载脂蛋白A-I(ApoA-I)是高密度脂蛋白(HDL)的主要蛋白质组分，高密度脂蛋白在将胆固醇从非肝组织转移回肝脏的过程中发挥着重要作用，从而在预防动脉粥样硬化方面发挥着关键作用。ApoA-I固有的灵活性使其结构能够适应不同种类的高密度脂蛋白的多种构象，这些高密度脂蛋白含有不同数量的磷脂和胆固醇。我们和其他人的研究表明，在无脂构象中，ApoA-I的N-末端和C-末端之间是非常接近的，因此存在相互作用。用质谱仪等方法研究了apoA-I的N端(残基1-44)和C端(残基198-243)两种多肽模型在无脂形式和脂结合形式下的构象和相互作用。一份描述我们结果的手稿正在准备中。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Previous work in our lab and data in the literature have consistently suggested that the Human apolipoprotein A-I (ApoA-I), is the principal protein component of high-density lipoprotein (HDL), which has a major function in transferring cholesterol from non-hepatic tissues back to the liver and thus plays a critical role in protection against atherosclerosis. The intrinsic flexibility of apoA-I allows its structure to adapt multiple conformations on different species of HDL that contain different amounts of phospholipids and cholesterol. Previous studies from our work and that of others has suggested the close proximity and thus the interaction between the N- and C-termini of ApoA-I in lipid- free conformation. The conformation and interaction of two peptide models, representing the N-terminal (residues 1-44) and C-terminal (residues 198-243) of apoA-I, have been investigated in lipid- free and lipid- bound forms by mass spectrometry and other methods. A manuscript describing our results is being prepared..